Activity-based probes as a tool for functional proteomic analysis of proteases.
Traditional proteomics methodology allows global analysis of protein abundance but does not provide information on the regulation of protein activity. Proteases, in particular, are known for their multilayered post-translational activity regulation that can lead to a significant difference between protease abundance levels and their enzyme activity. To address these issues, the field of activity-based proteomics has been established in order to characterize protein activity and monitor the functional regulation of enzymes in complex proteomes. In this review, we present structural features of activity-based probes for proteases and discuss their applications in proteomic profiling of various catalytic classes of proteases.
Fonović
Marko
M
Department of Biochemistry, Molecular and Structural Biology, JoZef Stefan Institute, Jamova Cesta 39, SI-1000 Ljubljana, Slovenia. marko.fonovic@ijs.si
Bogyo
Matthew
M
D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D045726:Metalloproteases / Q000737:chemistry / Q000378:metabolism; D015335:Molecular Probes / Q000737:chemistry*; D015394:Molecular Structure; D010447:Peptide Hydrolases / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism
D015335:Molecular Probes; D045726:Metalloproteases; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases